protease-free chondroitinase abc Search Results


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  • 99
    Millipore protease free chondroitinase abc
    Protease Free Chondroitinase Abc, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Seikagaku protease free chondroitinase abc
    Frame A: Zymograms showing <t>chondroitinase</t> <t>ABC</t> and testicular hyaluronidase digestions of the 230 and 72 kDa gelatinases. After digestion with either enzyme, 230 kDa gelatinase band showed a mobility shift, whereas no shift was observed for the 72 kDa
    Protease Free Chondroitinase Abc, supplied by Seikagaku, used in various techniques. Bioz Stars score: 89/100, based on 119 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Boehringer Mannheim protease free chondroitinase abc chabc
    NG2 Western blot of Neu7 detergent lysate after digestion of samples with various enzymes. No NG2 band at ∼300 kDa is seen in the absence of digestion with <t>chondroitinase</t> <t>ABC</t> or AC, but after digestion with these enzymes, a sharp band is seen. Chondroitinase ABC and AC produce the same effect, and there is no additive effect. In Neu7 detergent lysate, a larger unidentified band at higher molecular weight is also seen. On digestion with keratanase, the 300 kDa band disappears, and a new band is seen at 100 kDa. When chondroitinase ABC is added to the keratanase, a 200 kDa band is seen in addition to the 100 kDa band. Digestion overnight with keratanase and chondroitinase ( right lane ) leads to almost complete disappearance of the 200 kDa band.
    Protease Free Chondroitinase Abc Chabc, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Boehringer Mannheim protease free chondroitinase abc
    Myelin fractions enriched in proteoglycans do not support cell attachment and neurite outgrowth. Partially purified cerebellar granule neurons were seeded onto nitrocellulose-coated culture dishes absorbed with various myelin fractions as described in Material and Methods and were allowed to grow for 24 hr. The substrates are as follows: A, laminin (10 μg/ml); B, spinal cord myelin Chaps extract (10 μg/ml); C, spinal cord myelin Chaps extract (10 μg/ml) preincubated with the mAB IN-1 (1:1); D, proteoglycan-enriched myelin fraction (5 μg/ml); E, proteoglycan-enriched myelin fraction (5 μg/ml) preincubated with the mAB IN-1 (vol 1:1); F , proteoglycan-enriched myelin fraction after <t>chondroitinase</t> <t>ABC</t> treatment. Whereas cell attachment and neurite growth was extensive on laminin, there is reduced adhesion and outgrowth of cells on spinal-cord myelin extract or on a proteoglycan-enriched myelin fraction. Note that the mAB IN-1 could partially neutralize the effect of the spinal cord myelin extract but not of the proteoglycan-enriched myelin fraction. Treatment with chondroitinase ABC partially abolishes the latter activity. G , Quantification of neurite outgrowth of cerebellar granule cells on various substrates. The results are the mean ± SEM of five independent experiments. LN , Laminin-1; myelin , total myelin extract; PG , proteoglycan-enriched fraction. Scale bar, 50 μm.
    Protease Free Chondroitinase Abc, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 89/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Associates of Cape Cod Inc chondroitinase abc protease free
    Myelin fractions enriched in proteoglycans do not support cell attachment and neurite outgrowth. Partially purified cerebellar granule neurons were seeded onto nitrocellulose-coated culture dishes absorbed with various myelin fractions as described in Material and Methods and were allowed to grow for 24 hr. The substrates are as follows: A, laminin (10 μg/ml); B, spinal cord myelin Chaps extract (10 μg/ml); C, spinal cord myelin Chaps extract (10 μg/ml) preincubated with the mAB IN-1 (1:1); D, proteoglycan-enriched myelin fraction (5 μg/ml); E, proteoglycan-enriched myelin fraction (5 μg/ml) preincubated with the mAB IN-1 (vol 1:1); F , proteoglycan-enriched myelin fraction after <t>chondroitinase</t> <t>ABC</t> treatment. Whereas cell attachment and neurite growth was extensive on laminin, there is reduced adhesion and outgrowth of cells on spinal-cord myelin extract or on a proteoglycan-enriched myelin fraction. Note that the mAB IN-1 could partially neutralize the effect of the spinal cord myelin extract but not of the proteoglycan-enriched myelin fraction. Treatment with chondroitinase ABC partially abolishes the latter activity. G , Quantification of neurite outgrowth of cerebellar granule cells on various substrates. The results are the mean ± SEM of five independent experiments. LN , Laminin-1; myelin , total myelin extract; PG , proteoglycan-enriched fraction. Scale bar, 50 μm.
    Chondroitinase Abc Protease Free, supplied by Associates of Cape Cod Inc, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Seikagaku protease free chondrointinase abc
    Myelin fractions enriched in proteoglycans do not support cell attachment and neurite outgrowth. Partially purified cerebellar granule neurons were seeded onto nitrocellulose-coated culture dishes absorbed with various myelin fractions as described in Material and Methods and were allowed to grow for 24 hr. The substrates are as follows: A, laminin (10 μg/ml); B, spinal cord myelin Chaps extract (10 μg/ml); C, spinal cord myelin Chaps extract (10 μg/ml) preincubated with the mAB IN-1 (1:1); D, proteoglycan-enriched myelin fraction (5 μg/ml); E, proteoglycan-enriched myelin fraction (5 μg/ml) preincubated with the mAB IN-1 (vol 1:1); F , proteoglycan-enriched myelin fraction after <t>chondroitinase</t> <t>ABC</t> treatment. Whereas cell attachment and neurite growth was extensive on laminin, there is reduced adhesion and outgrowth of cells on spinal-cord myelin extract or on a proteoglycan-enriched myelin fraction. Note that the mAB IN-1 could partially neutralize the effect of the spinal cord myelin extract but not of the proteoglycan-enriched myelin fraction. Treatment with chondroitinase ABC partially abolishes the latter activity. G , Quantification of neurite outgrowth of cerebellar granule cells on various substrates. The results are the mean ± SEM of five independent experiments. LN , Laminin-1; myelin , total myelin extract; PG , proteoglycan-enriched fraction. Scale bar, 50 μm.
    Protease Free Chondrointinase Abc, supplied by Seikagaku, used in various techniques. Bioz Stars score: 80/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Seikagaku protease free chondroitinase abc chabc
    Myelin fractions enriched in proteoglycans do not support cell attachment and neurite outgrowth. Partially purified cerebellar granule neurons were seeded onto nitrocellulose-coated culture dishes absorbed with various myelin fractions as described in Material and Methods and were allowed to grow for 24 hr. The substrates are as follows: A, laminin (10 μg/ml); B, spinal cord myelin Chaps extract (10 μg/ml); C, spinal cord myelin Chaps extract (10 μg/ml) preincubated with the mAB IN-1 (1:1); D, proteoglycan-enriched myelin fraction (5 μg/ml); E, proteoglycan-enriched myelin fraction (5 μg/ml) preincubated with the mAB IN-1 (vol 1:1); F , proteoglycan-enriched myelin fraction after <t>chondroitinase</t> <t>ABC</t> treatment. Whereas cell attachment and neurite growth was extensive on laminin, there is reduced adhesion and outgrowth of cells on spinal-cord myelin extract or on a proteoglycan-enriched myelin fraction. Note that the mAB IN-1 could partially neutralize the effect of the spinal cord myelin extract but not of the proteoglycan-enriched myelin fraction. Treatment with chondroitinase ABC partially abolishes the latter activity. G , Quantification of neurite outgrowth of cerebellar granule cells on various substrates. The results are the mean ± SEM of five independent experiments. LN , Laminin-1; myelin , total myelin extract; PG , proteoglycan-enriched fraction. Scale bar, 50 μm.
    Protease Free Chondroitinase Abc Chabc, supplied by Seikagaku, used in various techniques. Bioz Stars score: 88/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Frame A: Zymograms showing chondroitinase ABC and testicular hyaluronidase digestions of the 230 and 72 kDa gelatinases. After digestion with either enzyme, 230 kDa gelatinase band showed a mobility shift, whereas no shift was observed for the 72 kDa

    Journal: Archives of biochemistry and biophysics

    Article Title: Matrix metalloproteinase-9 in a unique proteoglycan form in avian embryonic growth plate cartilage

    doi: 10.1016/j.abb.2012.02.003

    Figure Lengend Snippet: Frame A: Zymograms showing chondroitinase ABC and testicular hyaluronidase digestions of the 230 and 72 kDa gelatinases. After digestion with either enzyme, 230 kDa gelatinase band showed a mobility shift, whereas no shift was observed for the 72 kDa

    Article Snippet: 230 kDa enzyme was digested with protease-free chondroitinase ABC (40 μU) (Seikagaku Co., Tokyo, Japan) in chondroitinase buffer containing 50 mM Tris, pH 8.0, 30 mM sodium acetate, 0.02% (v/v) Brij-35, 0.02% (w/v) NaN3 and 0.05% (w/v) protease free BSA at 37°C for 2 h. Digested proteins were separated by SDS-PAGE and detected by Coomassie colloidal blue stain (OWL Separation Systems, Woburn, MA).

    Techniques: Mobility Shift

    MMP enzyme assay using peptide substrate. The effects of APMA activation and chondroitinase ABC treatment on the enzyme activity of the 230 kDa gelatinase were tested using a quenched fluorescent synthetic peptide substrate. APMA activated the latent

    Journal: Archives of biochemistry and biophysics

    Article Title: Matrix metalloproteinase-9 in a unique proteoglycan form in avian embryonic growth plate cartilage

    doi: 10.1016/j.abb.2012.02.003

    Figure Lengend Snippet: MMP enzyme assay using peptide substrate. The effects of APMA activation and chondroitinase ABC treatment on the enzyme activity of the 230 kDa gelatinase were tested using a quenched fluorescent synthetic peptide substrate. APMA activated the latent

    Article Snippet: 230 kDa enzyme was digested with protease-free chondroitinase ABC (40 μU) (Seikagaku Co., Tokyo, Japan) in chondroitinase buffer containing 50 mM Tris, pH 8.0, 30 mM sodium acetate, 0.02% (v/v) Brij-35, 0.02% (w/v) NaN3 and 0.05% (w/v) protease free BSA at 37°C for 2 h. Digested proteins were separated by SDS-PAGE and detected by Coomassie colloidal blue stain (OWL Separation Systems, Woburn, MA).

    Techniques: Enzymatic Assay, Activation Assay, Activity Assay

    Macromolecular composition of the 230 kDa gelatinase. Frame A shows a chondroitinase ABC digestion of the 230 kDa gelatinase on SDS-PAGE stained with Coomassie colloidal blue stain. Lanes M, molecular weight standards; 1, chondroitinase ABC enzyme alone;

    Journal: Archives of biochemistry and biophysics

    Article Title: Matrix metalloproteinase-9 in a unique proteoglycan form in avian embryonic growth plate cartilage

    doi: 10.1016/j.abb.2012.02.003

    Figure Lengend Snippet: Macromolecular composition of the 230 kDa gelatinase. Frame A shows a chondroitinase ABC digestion of the 230 kDa gelatinase on SDS-PAGE stained with Coomassie colloidal blue stain. Lanes M, molecular weight standards; 1, chondroitinase ABC enzyme alone;

    Article Snippet: 230 kDa enzyme was digested with protease-free chondroitinase ABC (40 μU) (Seikagaku Co., Tokyo, Japan) in chondroitinase buffer containing 50 mM Tris, pH 8.0, 30 mM sodium acetate, 0.02% (v/v) Brij-35, 0.02% (w/v) NaN3 and 0.05% (w/v) protease free BSA at 37°C for 2 h. Digested proteins were separated by SDS-PAGE and detected by Coomassie colloidal blue stain (OWL Separation Systems, Woburn, MA).

    Techniques: SDS Page, Staining, Molecular Weight

    Influence of TIMPs and chondroitinase ABC treatment on 230 kDa gelatinase activity. In all assays the 230 kDa gelatinase was APMA activated and incubated with the peptide substrate in presence of 500 ng of TIMP-1 or TIMP-2 either without (frame A) or

    Journal: Archives of biochemistry and biophysics

    Article Title: Matrix metalloproteinase-9 in a unique proteoglycan form in avian embryonic growth plate cartilage

    doi: 10.1016/j.abb.2012.02.003

    Figure Lengend Snippet: Influence of TIMPs and chondroitinase ABC treatment on 230 kDa gelatinase activity. In all assays the 230 kDa gelatinase was APMA activated and incubated with the peptide substrate in presence of 500 ng of TIMP-1 or TIMP-2 either without (frame A) or

    Article Snippet: 230 kDa enzyme was digested with protease-free chondroitinase ABC (40 μU) (Seikagaku Co., Tokyo, Japan) in chondroitinase buffer containing 50 mM Tris, pH 8.0, 30 mM sodium acetate, 0.02% (v/v) Brij-35, 0.02% (w/v) NaN3 and 0.05% (w/v) protease free BSA at 37°C for 2 h. Digested proteins were separated by SDS-PAGE and detected by Coomassie colloidal blue stain (OWL Separation Systems, Woburn, MA).

    Techniques: Activity Assay, Incubation

    GPC1 expression in tumor xenografts. ( A ) Immunoblotting. Tumors from sham-transfected and GAS PANC-1 cells (GAS6 and GAS7) were homogenized and incubated with control buffer, heparitinase, or heparitinase and chondroitinase ABC (Ch-ABC). Protein lysates were subjected to immunoblotting using affinity-purified rabbit anti-GPC1 antibody as reported in Methods. Membranes from cell lysates were reprobed with an anti-ERK2 antibody to confirm equivalent loading of lanes. ( B ) Densitometric analysis. Frozen lysates for immunoblotting from 6 sham, 5 GAS6, and 4 GAS7 tumors were subjected to densitometry. * P

    Journal: The Journal of Clinical Investigation

    Article Title: Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells

    doi: 10.1172/JCI32412

    Figure Lengend Snippet: GPC1 expression in tumor xenografts. ( A ) Immunoblotting. Tumors from sham-transfected and GAS PANC-1 cells (GAS6 and GAS7) were homogenized and incubated with control buffer, heparitinase, or heparitinase and chondroitinase ABC (Ch-ABC). Protein lysates were subjected to immunoblotting using affinity-purified rabbit anti-GPC1 antibody as reported in Methods. Membranes from cell lysates were reprobed with an anti-ERK2 antibody to confirm equivalent loading of lanes. ( B ) Densitometric analysis. Frozen lysates for immunoblotting from 6 sham, 5 GAS6, and 4 GAS7 tumors were subjected to densitometry. * P

    Article Snippet: The following materials were purchased from the following companies: DMEM, RPMI 1640, and trypsin-EDTA from Mediatech Inc.; FBS from Omega Scientific Inc.; G418 from GIBCO Laboratories; Noble agar from Difco Laboratories; recombinant human EGF from Chemicon; Heparitinase and Chondroitinase ABC Protease Free from Seikagaku Corporation; One Solution reagent and anti–phospho-MAPK antibody from Promega; Immobilon-P PVDF membranes from Millipore Corp.; RNeasy Mini Kit from Qiagen; phosphatidylinositol-specific phospholipase C (PI-PLC) from Molecular Probes; magnetic dynabeads from Dynal Biotech from Invitrogen; SulfoLink Coupling Gel from Pierce Biotechnology; anti–ERK-2 antibody, anti–angiopoietin-1 and -2 antibodies, and anti-Tie2 antibody from Santa Cruz Biotechnology Inc.; anti-CD31 rat anti-mouse monoclonal antibody (catalog no. 553370) and anti-VE cadherin antibody from Pharmingen; anti-PCNA monoclonal antibody from Novocastra; Antigen Unmasking Solution from Vector Laboratories; ApopTag in situ apoptosis detection kit from Chemicon; oligonucleotide primers from Applied Biosystems; PANC-1 human pancreatic cancer cells and COS-7 cells from American Type Culture Collection.

    Techniques: Expressing, Transfection, Incubation, Affinity Purification

    Effects of GPC1 antisense expression on GPC1 protein levels. ( A ) Effects of enzymatic treatment on immunoblotting. Sham-transfected cells and GPC1 antisense–expressing cells (clone GAS6) were incubated in the absence or presence of the indicated enzymes and subjected to immunoblotting using affinity-purified rabbit anti-GPC1 antibody as reported in Methods. ( B ) Total cell lysates from sham-transfected and from both antisense-expressing clones as well as the corresponding conditioned media were incubated with heparitinase and chondroitinase ABC and subjected to immunoblotting as described above. Membranes from cell lysates were reprobed with an anti-ERK2 antibody to confirm equivalent loading of lanes. Each panel is representative of 2 distinct experiments.

    Journal: The Journal of Clinical Investigation

    Article Title: Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells

    doi: 10.1172/JCI32412

    Figure Lengend Snippet: Effects of GPC1 antisense expression on GPC1 protein levels. ( A ) Effects of enzymatic treatment on immunoblotting. Sham-transfected cells and GPC1 antisense–expressing cells (clone GAS6) were incubated in the absence or presence of the indicated enzymes and subjected to immunoblotting using affinity-purified rabbit anti-GPC1 antibody as reported in Methods. ( B ) Total cell lysates from sham-transfected and from both antisense-expressing clones as well as the corresponding conditioned media were incubated with heparitinase and chondroitinase ABC and subjected to immunoblotting as described above. Membranes from cell lysates were reprobed with an anti-ERK2 antibody to confirm equivalent loading of lanes. Each panel is representative of 2 distinct experiments.

    Article Snippet: The following materials were purchased from the following companies: DMEM, RPMI 1640, and trypsin-EDTA from Mediatech Inc.; FBS from Omega Scientific Inc.; G418 from GIBCO Laboratories; Noble agar from Difco Laboratories; recombinant human EGF from Chemicon; Heparitinase and Chondroitinase ABC Protease Free from Seikagaku Corporation; One Solution reagent and anti–phospho-MAPK antibody from Promega; Immobilon-P PVDF membranes from Millipore Corp.; RNeasy Mini Kit from Qiagen; phosphatidylinositol-specific phospholipase C (PI-PLC) from Molecular Probes; magnetic dynabeads from Dynal Biotech from Invitrogen; SulfoLink Coupling Gel from Pierce Biotechnology; anti–ERK-2 antibody, anti–angiopoietin-1 and -2 antibodies, and anti-Tie2 antibody from Santa Cruz Biotechnology Inc.; anti-CD31 rat anti-mouse monoclonal antibody (catalog no. 553370) and anti-VE cadherin antibody from Pharmingen; anti-PCNA monoclonal antibody from Novocastra; Antigen Unmasking Solution from Vector Laboratories; ApopTag in situ apoptosis detection kit from Chemicon; oligonucleotide primers from Applied Biosystems; PANC-1 human pancreatic cancer cells and COS-7 cells from American Type Culture Collection.

    Techniques: Expressing, Transfection, Incubation, Affinity Purification, Clone Assay

    NG2 Western blot of Neu7 detergent lysate after digestion of samples with various enzymes. No NG2 band at ∼300 kDa is seen in the absence of digestion with chondroitinase ABC or AC, but after digestion with these enzymes, a sharp band is seen. Chondroitinase ABC and AC produce the same effect, and there is no additive effect. In Neu7 detergent lysate, a larger unidentified band at higher molecular weight is also seen. On digestion with keratanase, the 300 kDa band disappears, and a new band is seen at 100 kDa. When chondroitinase ABC is added to the keratanase, a 200 kDa band is seen in addition to the 100 kDa band. Digestion overnight with keratanase and chondroitinase ( right lane ) leads to almost complete disappearance of the 200 kDa band.

    Journal: The Journal of Neuroscience

    Article Title: Comparing Astrocytic Cell Lines that Are Inhibitory or Permissive for Axon Growth: the Major Axon-Inhibitory Proteoglycan Is NG2

    doi: 10.1523/JNEUROSCI.19-20-08778.1999

    Figure Lengend Snippet: NG2 Western blot of Neu7 detergent lysate after digestion of samples with various enzymes. No NG2 band at ∼300 kDa is seen in the absence of digestion with chondroitinase ABC or AC, but after digestion with these enzymes, a sharp band is seen. Chondroitinase ABC and AC produce the same effect, and there is no additive effect. In Neu7 detergent lysate, a larger unidentified band at higher molecular weight is also seen. On digestion with keratanase, the 300 kDa band disappears, and a new band is seen at 100 kDa. When chondroitinase ABC is added to the keratanase, a 200 kDa band is seen in addition to the 100 kDa band. Digestion overnight with keratanase and chondroitinase ( right lane ) leads to almost complete disappearance of the 200 kDa band.

    Article Snippet: Samples of 0.05 ml were digested with 0.02 U of protease-free chondroitinase ABC (ChABC) (Boehringer Mannheim) for 2.5 hr at 37°C.

    Techniques: Western Blot, Molecular Weight

    Myelin fractions enriched in proteoglycans do not support cell attachment and neurite outgrowth. Partially purified cerebellar granule neurons were seeded onto nitrocellulose-coated culture dishes absorbed with various myelin fractions as described in Material and Methods and were allowed to grow for 24 hr. The substrates are as follows: A, laminin (10 μg/ml); B, spinal cord myelin Chaps extract (10 μg/ml); C, spinal cord myelin Chaps extract (10 μg/ml) preincubated with the mAB IN-1 (1:1); D, proteoglycan-enriched myelin fraction (5 μg/ml); E, proteoglycan-enriched myelin fraction (5 μg/ml) preincubated with the mAB IN-1 (vol 1:1); F , proteoglycan-enriched myelin fraction after chondroitinase ABC treatment. Whereas cell attachment and neurite growth was extensive on laminin, there is reduced adhesion and outgrowth of cells on spinal-cord myelin extract or on a proteoglycan-enriched myelin fraction. Note that the mAB IN-1 could partially neutralize the effect of the spinal cord myelin extract but not of the proteoglycan-enriched myelin fraction. Treatment with chondroitinase ABC partially abolishes the latter activity. G , Quantification of neurite outgrowth of cerebellar granule cells on various substrates. The results are the mean ± SEM of five independent experiments. LN , Laminin-1; myelin , total myelin extract; PG , proteoglycan-enriched fraction. Scale bar, 50 μm.

    Journal: The Journal of Neuroscience

    Article Title: Bovine CNS Myelin Contains Neurite Growth-Inhibitory Activity Associated with Chondroitin Sulfate Proteoglycans

    doi: 10.1523/JNEUROSCI.19-20-08979.1999

    Figure Lengend Snippet: Myelin fractions enriched in proteoglycans do not support cell attachment and neurite outgrowth. Partially purified cerebellar granule neurons were seeded onto nitrocellulose-coated culture dishes absorbed with various myelin fractions as described in Material and Methods and were allowed to grow for 24 hr. The substrates are as follows: A, laminin (10 μg/ml); B, spinal cord myelin Chaps extract (10 μg/ml); C, spinal cord myelin Chaps extract (10 μg/ml) preincubated with the mAB IN-1 (1:1); D, proteoglycan-enriched myelin fraction (5 μg/ml); E, proteoglycan-enriched myelin fraction (5 μg/ml) preincubated with the mAB IN-1 (vol 1:1); F , proteoglycan-enriched myelin fraction after chondroitinase ABC treatment. Whereas cell attachment and neurite growth was extensive on laminin, there is reduced adhesion and outgrowth of cells on spinal-cord myelin extract or on a proteoglycan-enriched myelin fraction. Note that the mAB IN-1 could partially neutralize the effect of the spinal cord myelin extract but not of the proteoglycan-enriched myelin fraction. Treatment with chondroitinase ABC partially abolishes the latter activity. G , Quantification of neurite outgrowth of cerebellar granule cells on various substrates. The results are the mean ± SEM of five independent experiments. LN , Laminin-1; myelin , total myelin extract; PG , proteoglycan-enriched fraction. Scale bar, 50 μm.

    Article Snippet: Proteoglycan-enriched fractions were digested with protease-free chondroitinase ABC (Boehringer Mannheim, Indianapolis, IN) in 40 m m Tris, pH 8.0, 40 m m sodium acetate, and 0.1 mg/ml BSA.

    Techniques: Cell Attachment Assay, Purification, Activity Assay

    Presence of brevican and versican in proteoglycan-enriched myelin fraction. Aliquots of peak III activity pool (5 μg each) without ( lanes 1 , 3 , 5 ) or with ( lanes 2 , 4 , 6 ) chondroitinase ABC digestion were electrophoresed on 5 or 6% SDS-polyacrylamide gels under nonreducing conditions and immunoblotted with anti-GAGα (1:1000) recognizing V2/V0 bovine versican, GAGβ (1:1000) recognizing V1/V0 bovine versican, and anti-brevican antibodies (1:1000).

    Journal: The Journal of Neuroscience

    Article Title: Bovine CNS Myelin Contains Neurite Growth-Inhibitory Activity Associated with Chondroitin Sulfate Proteoglycans

    doi: 10.1523/JNEUROSCI.19-20-08979.1999

    Figure Lengend Snippet: Presence of brevican and versican in proteoglycan-enriched myelin fraction. Aliquots of peak III activity pool (5 μg each) without ( lanes 1 , 3 , 5 ) or with ( lanes 2 , 4 , 6 ) chondroitinase ABC digestion were electrophoresed on 5 or 6% SDS-polyacrylamide gels under nonreducing conditions and immunoblotted with anti-GAGα (1:1000) recognizing V2/V0 bovine versican, GAGβ (1:1000) recognizing V1/V0 bovine versican, and anti-brevican antibodies (1:1000).

    Article Snippet: Proteoglycan-enriched fractions were digested with protease-free chondroitinase ABC (Boehringer Mannheim, Indianapolis, IN) in 40 m m Tris, pH 8.0, 40 m m sodium acetate, and 0.1 mg/ml BSA.

    Techniques: Activity Assay